EP0145092A2 - Verfahren zur Herstellung einer keimfreien Lösung eines Laktose spaltenden Enzyms und deren Verwendung - Google Patents
Verfahren zur Herstellung einer keimfreien Lösung eines Laktose spaltenden Enzyms und deren Verwendung Download PDFInfo
- Publication number
- EP0145092A2 EP0145092A2 EP84201779A EP84201779A EP0145092A2 EP 0145092 A2 EP0145092 A2 EP 0145092A2 EP 84201779 A EP84201779 A EP 84201779A EP 84201779 A EP84201779 A EP 84201779A EP 0145092 A2 EP0145092 A2 EP 0145092A2
- Authority
- EP
- European Patent Office
- Prior art keywords
- lactose
- enzyme
- solution
- germ
- sterile
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 51
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 51
- 238000000034 method Methods 0.000 title claims abstract description 30
- 238000002360 preparation method Methods 0.000 title claims abstract description 8
- 235000013336 milk Nutrition 0.000 claims abstract description 29
- 239000008267 milk Substances 0.000 claims abstract description 29
- 210000004080 milk Anatomy 0.000 claims abstract description 29
- 239000000047 product Substances 0.000 claims abstract description 19
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 claims abstract description 15
- 238000011146 sterile filtration Methods 0.000 claims abstract description 14
- 239000008101 lactose Substances 0.000 claims abstract description 13
- 238000000746 purification Methods 0.000 claims abstract description 10
- 238000011084 recovery Methods 0.000 claims abstract description 10
- 238000000855 fermentation Methods 0.000 claims abstract description 6
- 230000004151 fermentation Effects 0.000 claims abstract description 6
- 239000007857 degradation product Substances 0.000 claims abstract description 4
- 230000015572 biosynthetic process Effects 0.000 claims abstract description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 claims description 36
- 239000000654 additive Substances 0.000 claims description 5
- 239000002904 solvent Substances 0.000 claims description 5
- 229940088598 enzyme Drugs 0.000 description 40
- 239000000243 solution Substances 0.000 description 36
- 108010059881 Lactase Proteins 0.000 description 13
- 108010005774 beta-Galactosidase Proteins 0.000 description 13
- 102100026189 Beta-galactosidase Human genes 0.000 description 12
- 238000001914 filtration Methods 0.000 description 12
- 229940116108 lactase Drugs 0.000 description 12
- 230000001954 sterilising effect Effects 0.000 description 8
- 238000004659 sterilization and disinfection Methods 0.000 description 8
- 235000013365 dairy product Nutrition 0.000 description 7
- 235000020191 long-life milk Nutrition 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 239000012528 membrane Substances 0.000 description 5
- 239000011148 porous material Substances 0.000 description 5
- 230000015556 catabolic process Effects 0.000 description 4
- 238000006731 degradation reaction Methods 0.000 description 4
- 208000035404 Autolysis Diseases 0.000 description 3
- 206010057248 Cell death Diseases 0.000 description 3
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 3
- 201000010538 Lactose Intolerance Diseases 0.000 description 3
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 239000008103 glucose Substances 0.000 description 3
- 238000012856 packing Methods 0.000 description 3
- 230000028043 self proteolysis Effects 0.000 description 3
- 238000000108 ultra-filtration Methods 0.000 description 3
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 2
- 239000012141 concentrate Substances 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 229930182830 galactose Natural products 0.000 description 2
- 230000036512 infertility Effects 0.000 description 2
- 230000000968 intestinal effect Effects 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 238000009928 pasteurization Methods 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- 206010053567 Coagulopathies Diseases 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 102000014171 Milk Proteins Human genes 0.000 description 1
- 108010011756 Milk Proteins Proteins 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 108010051210 beta-Fructofuranosidase Proteins 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 239000003610 charcoal Substances 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 230000035602 clotting Effects 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 210000002249 digestive system Anatomy 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 239000001573 invertase Substances 0.000 description 1
- 235000011073 invertase Nutrition 0.000 description 1
- 235000020190 lactose-free milk Nutrition 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 235000021239 milk protein Nutrition 0.000 description 1
- 150000002772 monosaccharides Chemical class 0.000 description 1
- 235000020200 pasteurised milk Nutrition 0.000 description 1
- 238000010935 polish filtration Methods 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 238000011045 prefiltration Methods 0.000 description 1
- CMDGQTVYVAKDNA-UHFFFAOYSA-N propane-1,2,3-triol;hydrate Chemical compound O.OCC(O)CO CMDGQTVYVAKDNA-UHFFFAOYSA-N 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01108—Lactase (3.2.1.108)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2468—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1) acting on beta-galactose-glycoside bonds, e.g. carrageenases (3.2.1.83; 3.2.1.157); beta-agarase (3.2.1.81)
- C12N9/2471—Beta-galactosidase (3.2.1.23), i.e. exo-(1-->4)-beta-D-galactanase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/78—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
- C12N9/86—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5) acting on amide bonds in cyclic amides, e.g. penicillinase (3.5.2)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01023—Beta-galactosidase (3.2.1.23), i.e. exo-(1-->4)-beta-D-galactanase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y305/00—Hydrolases acting on carbon-nitrogen bonds, other than peptide bonds (3.5)
- C12Y305/02—Hydrolases acting on carbon-nitrogen bonds, other than peptide bonds (3.5) in cyclic amides (3.5.2)
- C12Y305/02006—Beta-lactamase (3.5.2.6)
Definitions
- This invention relates to a process for the preparation of a germ-free solution of a lactose-splitting enzyme, and to its use in preparing milk and milk products with a reduced lactose content.
- Lactose (milk sugar) is a disaccharide present in dairy products and more particularly in milk, skimmed milk, cream and other milk products. These products contain lactose in an amount of approximately 4-5%.
- the non-absorbable lactose is usually broken down in the body into the absorbable monosaccharides glucose and galactose. This break-down is generally brought about by a natural enzyme, named p-galactosidase or lactase, present in the intestinal wall in the human body (and in other mammals).
- lactose-intolerance which is caused by the total or partial absence from their digestive system of lactase for the break-down of lactose-containing products. Therefore the lactose is either not broken down, or is insufficiently broken down into glucose and galactose which can be absorbed: the non-absorbable lactose then causes intestinal trouble.
- lactose intolerance has been recognized for many years. Because of its amino acid constitution milk protein has a large food value. Attempts have been made to prepare lactose-poor or lactose-free milk and milk products for sufferers from lactose intolerance by adding lactase to milk and milk products. An extra advantage of the addition of lactase may be that the products treated in this way are sweeter.
- the germ-poor lactase usually supplied to the dairy processing industry in an aqueous solution to which one or more stabilizing agents, e.g. glycerol, are added, is filtered before use.
- the filtered enzyme solution is pumped through a sterile filter, injected via a dosing device into a production line of previously sterilized milk and then mixed with the milk. Finally the mixture is divided and packed under aseptic conditions in uniform packs.
- the sterile filter often blocks.
- the blockages are mostly due to degradation of proteins and polysaccharides (gums), which may remain in the enzyme solution in spite of the purification.
- the degradation phenomena generally increase the longer the enzyme is kept prior to use and may be promoted because there may be a considerable period of time between the production of the enzyme by the enzyme manufacturer and its use by the dairy processing industry.
- Protease present in the lactase may also play a role in the degradation processes.
- the invention therefore provides a process for the preparation of a germ-free solution of a lactose-splitting enzyme characterized in that a solution of the lactose-splitting enzyme is made germ-free by sterile filtration after the recovery and purification of a solution of lactose-splitting enzyme produced by fermentation, but before the formation of degradation products sufficient to clog the sterile filter.
- the process according to the invention has the additional advantage that the sterilization of the enzyme solution can be carried out by the enzyme producer himself.
- the different dairy processing industries each used to subject the enzyme solution supplied to sterile filtration or possibly sterilized it in another way.
- the enzyme solution can be made germ-free by any known methods which all fall within the scope of the invention.
- the enzyme solution is made germ-poor before it is subjected to sterile filtration. It is preferred to make the solution germ-poor with a germ reduction filter, for instance SEITZ Supra EKS filter pads. It is preferable to make the solution germ-poor immediately after the aforementioned steps.
- the solution is also subjected to ultrafiltration to concentrate the enzyme before sterile filtration.
- the sterile filtration is preferably carried out with one or more membrane filters.
- a suitable filter is for instance a membrane filter with a pore size of 0.22 pm.
- the timing of the germ filtration of the enzyme solution is not critical but should be chosen so that no considerable amount of degradation products has yet been formed to cause clogging of the filter. It is therefore recommended to carry out the germ filtration shortly after the recovery and purification.
- the germ filtration is carried out within 14 days and more preferably within 5 days of the recovery and purification.
- solvents or other additives may be added, for example to bring the enzyme activity to the desired level and to further stabilize the enzyme.
- Suitable solvents are, for example, sorbitol and glycerol.
- Suitable additives, which stabilize the enzyme are, for example, hydrolysed lactose, glucose, mannitol and salt buffers.
- additives may be added to sweeten further the milk and milk products.
- Such additive is, for example, invertase, which may be added to or is already present in the enzyme solution.
- the addition is carried out after the sterilization, the added compounds being of course previously sterilized.
- a preferred solvent, which at the same time contributes to the stabilization of the enzyme is glycerol.
- the final glycerol-water ratio is not critical but is preferably between 1:9 and 4:1 by volume, and particularly between 1:3 and 1:1.
- an aqueous fermentation product containing lactase is subjected to autolysis and subsequently filtered, preferably with filter aids. If necessary, the filtrate is treated with active charcoal, and passed through a germ reduction filter (a so-called polish filter) to make the solution germ-poor. Ultrafiltration then takes place to concentrate the enzyme, after which glycerol is added (about 50 wt.%).
- the solution thus obtained is again passed through a germ reduction filter (SEITZ Supra EKS filter pads) and then in line through a sterile filter (a membrane filter with a pore size of 0.22,um). Finally the solution is passed into a sterile container which is immediately sealed.
- glycerol in another suitable embodiment about 20 wt.% of glycerol is added to the filtrate, after the autolysis, filtration, polish filtration and ultrafiltration as described above.
- the solution obtained is then passed through a germ reduction filter and subsequently through a sterile filter.
- the solution is then adjusted to the required concentration (about 1:1) with sterile glycerol and is packed under sterile conditions.
- the invention further relates to a process for the preparation of milk or a milk product with a reduced lactose content (which also means a sweeter product) by adding a germ-free solution of a lactose-splitting enzyme, prepared by the process of the invention.
- the sterile enzyme solution can be preserved in a sterile container before being used by the dairy processing industry.
- Sterile containers in which liquids may be preserved have been described frequently in the literature.
- a container is used which can be easily connected to the dosing pump into a milk production line, for instance as described in the previously mentioned article in the journal Voedingsmiddelentechnologie.
- the connection of the container to the dosage pump must, of course, be carried out under germ-free circumstances.
- the sterile filter between the sterile enzyme solution and the production line as described in the processes of the prior art can be omitted when a germ-free solution of enzyme obtained by a process according to the invention is employed. Precipitate which may occur because of degradation processes does not clog the dosage pump and is totally harmless in nature.
- the enzyme concentration in the milk is so low that the amount of precipitate in the final product is insignificant.
- a solution containing 50 wt.% glycerol was used in a test in a dairy plant. This solution was injected via a dosing device in a production line of previously sterilized milk and mixed in a mixer with the milk. Finally, the mixture was divided and packed under aseptic conditions in packages of 1 litre.
- the sterility of the milk after 7 days storage at 30'C was 100%. More than 85% of the lactose was hydrolysed.
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Enzymes And Modification Thereof (AREA)
- Dairy Products (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Medicinal Preparation (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Separation Using Semi-Permeable Membranes (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AT84201779T ATE30048T1 (de) | 1983-12-02 | 1984-11-30 | Verfahren zur herstellung einer keimfreien loesung eines laktose spaltenden enzyms und deren verwendung. |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| NL8304153 | 1983-12-02 | ||
| NL8304153 | 1983-12-02 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| EP0145092A2 true EP0145092A2 (de) | 1985-06-19 |
| EP0145092A3 EP0145092A3 (en) | 1985-07-17 |
| EP0145092B1 EP0145092B1 (de) | 1987-09-30 |
Family
ID=19842816
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EP84201779A Expired EP0145092B1 (de) | 1983-12-02 | 1984-11-30 | Verfahren zur Herstellung einer keimfreien Lösung eines Laktose spaltenden Enzyms und deren Verwendung |
Country Status (13)
| Country | Link |
|---|---|
| EP (1) | EP0145092B1 (de) |
| JP (1) | JPH0673454B2 (de) |
| AT (1) | ATE30048T1 (de) |
| AU (1) | AU586809B2 (de) |
| CA (1) | CA1246476A (de) |
| DE (1) | DE3466559D1 (de) |
| DK (1) | DK166734B1 (de) |
| ES (1) | ES8601302A1 (de) |
| FI (1) | FI83433C (de) |
| GR (1) | GR81128B (de) |
| IE (1) | IE57875B1 (de) |
| NZ (1) | NZ210391A (de) |
| PT (1) | PT79594B (de) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2002081673A1 (en) * | 2001-04-04 | 2002-10-17 | Dsm Ip Assets B.V. | Purified lactase |
| WO2018130654A1 (en) * | 2017-01-13 | 2018-07-19 | Novozymes A/S | Sterile filtered lactase preparation comprising salt with monovalent cation |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5618689A (en) * | 1995-05-25 | 1997-04-08 | Nestec S.A. | Enhanced procedures for preparing food hydrolysates |
| JPWO2021210659A1 (de) | 2020-04-17 | 2021-10-21 |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB1477087A (en) * | 1974-11-13 | 1977-06-22 | Tetra Pak Int | Treatment of dairy products |
-
1984
- 1984-11-27 AU AU35906/84A patent/AU586809B2/en not_active Ceased
- 1984-11-30 FI FI844737A patent/FI83433C/fi not_active IP Right Cessation
- 1984-11-30 DE DE8484201779T patent/DE3466559D1/de not_active Expired
- 1984-11-30 NZ NZ210391A patent/NZ210391A/xx unknown
- 1984-11-30 EP EP84201779A patent/EP0145092B1/de not_active Expired
- 1984-11-30 DK DK570984A patent/DK166734B1/da not_active IP Right Cessation
- 1984-11-30 ES ES538184A patent/ES8601302A1/es not_active Expired
- 1984-11-30 JP JP59253904A patent/JPH0673454B2/ja not_active Expired - Lifetime
- 1984-11-30 PT PT79594A patent/PT79594B/pt not_active IP Right Cessation
- 1984-11-30 CA CA000469084A patent/CA1246476A/en not_active Expired
- 1984-11-30 IE IE3064/84A patent/IE57875B1/en not_active IP Right Cessation
- 1984-11-30 AT AT84201779T patent/ATE30048T1/de not_active IP Right Cessation
- 1984-11-30 GR GR81128A patent/GR81128B/el unknown
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB1477087A (en) * | 1974-11-13 | 1977-06-22 | Tetra Pak Int | Treatment of dairy products |
Non-Patent Citations (4)
| Title |
|---|
| CHEMICAL ABSTRACTS, vol. 99, no. 19, November 1983, page 506, no. 157093z, Columbus, Ohio, US; & SE - A - 428 257 (TETRA PAK INTERNATIONAL AB) 20-06-1983 * |
| FOOD SCIENCE & TECHNOLOGY ABSTRACTS, abstract no. 78003500, Dep. of Food Sci., Chem. Cent., Univ. of Lund, Lund, SE; A. DAHLQVIST et al.: "Hydrolysis of lactose in milk and whey with minute amounts of lactase" & JOURNAL OF DAIRY RESEARCH, vol. 44, no. 3, 1977, pages 541-548 * |
| FOOD SCIENCE & TECHNOLOGY ABSTRACTS, abstract no. 79051743, Gist-Brocades NV, Delft, NL; H.H. NIJPELS: "Maxilact: milk for millions. Why milk with a low lactose content ?" & WORLD GALAXY, no. 7, pages 39-41 * |
| VOEDINGSMIDDELEN TECHNOLOGIE, vol. 13, no. 5, March 1970, page 23, Zeist, NL; "Melk met gereduceerd lactose gehalte" * |
Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2002081673A1 (en) * | 2001-04-04 | 2002-10-17 | Dsm Ip Assets B.V. | Purified lactase |
| EP2280065A1 (de) | 2001-04-04 | 2011-02-02 | DSM IP Assets B.V. | Gereinigte Lactase |
| US7955831B2 (en) | 2001-04-04 | 2011-06-07 | Dsm Ip Assets B.V. | Purified lactase |
| US9149048B2 (en) | 2001-04-04 | 2015-10-06 | Dsm Ip Assets B.V. | Purified lactase |
| EP1373491B1 (de) | 2001-04-04 | 2015-12-30 | DSM IP Assets B.V. | Gereinigte lactase |
| US9763460B2 (en) | 2001-04-04 | 2017-09-19 | Dsm Ip Assets B.V. | Purified lactase |
| WO2018130654A1 (en) * | 2017-01-13 | 2018-07-19 | Novozymes A/S | Sterile filtered lactase preparation comprising salt with monovalent cation |
| EP3568023B1 (de) | 2017-01-13 | 2021-07-07 | Novozymes A/S | Sterilfiltrierte laktasezubereitung enthaltend salz mit einem monovalenten kation und deren herstellung |
| US11576393B2 (en) | 2017-01-13 | 2023-02-14 | Novozymes A/S | Sterile filtered lactase preparation comprising salt with monovalent cation |
Also Published As
| Publication number | Publication date |
|---|---|
| DK570984D0 (da) | 1984-11-30 |
| FI83433B (fi) | 1991-03-28 |
| IE843064L (en) | 1985-06-02 |
| FI83433C (fi) | 1991-07-10 |
| ATE30048T1 (de) | 1987-10-15 |
| FI844737A0 (fi) | 1984-11-30 |
| GR81128B (en) | 1985-04-01 |
| DK570984A (da) | 1985-06-03 |
| CA1246476A (en) | 1988-12-13 |
| JPS60145085A (ja) | 1985-07-31 |
| NZ210391A (en) | 1988-08-30 |
| JPH0673454B2 (ja) | 1994-09-21 |
| EP0145092B1 (de) | 1987-09-30 |
| DK166734B1 (da) | 1993-07-05 |
| PT79594B (en) | 1986-09-11 |
| FI844737L (fi) | 1985-06-03 |
| EP0145092A3 (en) | 1985-07-17 |
| AU3590684A (en) | 1985-06-06 |
| ES538184A0 (es) | 1985-11-01 |
| ES8601302A1 (es) | 1985-11-01 |
| PT79594A (en) | 1984-12-01 |
| IE57875B1 (en) | 1993-05-05 |
| AU586809B2 (en) | 1989-07-27 |
| DE3466559D1 (en) | 1987-11-05 |
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